Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6MSF

F6 APTAMER MS2 COAT PROTEIN COMPLEX

Summary for 6MSF
Entry DOI10.2210/pdb6msf/pdb
DescriptorRNA (5'-R(*CP*CP*AP*CP*AP*GP*UP*CP*AP*CP*UP*GP*GP*G)-3'), RNA (5'-R(*CP*AP*GP*UP*CP*AP*CP*UP*GP*G)-3'), PROTEIN (MS2 PROTEIN CAPSID), ... (4 entities in total)
Functional Keywordsviral coat protein-rna complex, rna aptamer, rna stem loop, bacteriophage ms2, icosahedral virus, virus-rna complex, virus/rna
Biological sourceEnterobacterio phage MS2
Cellular locationVirion (Potential): P03612
Total number of polymer chains5
Total formula weight48854.06
Authors
Convery, M.A.,Rowsell, S.,Stonehouse, N.J.,Ellington, A.D.,Hirao, I.,Murray, J.B.,Peabody, D.S.,Phillips, S.E.V.,Stockley, P.G. (deposition date: 1998-01-06, release date: 1998-07-08, Last modification date: 2023-08-02)
Primary citationConvery, M.A.,Rowsell, S.,Stonehouse, N.J.,Ellington, A.D.,Hirao, I.,Murray, J.B.,Peabody, D.S.,Phillips, S.E.,Stockley, P.G.
Crystal structure of an RNA aptamer-protein complex at 2.8 A resolution.
Nat.Struct.Biol., 5:133-139, 1998
Cited by
PubMed Abstract: The crystal structure, at 2.8 A resolution, of an RNA aptamer bound to bacteriophage MS2 coat protein has been determined. It provides an opportunity to compare the interactions of MS2 coat protein and wild type operator with those of an aptamer, whose secondary structure differs from the wild type RNA in having a three-base loop (compared to a tetraloop) and an additional base pair between this loop and the sequence-specific recognition element in the stem. The RNA binds in the same location on the coat protein as the wild type operator and maintains many of the same RNA-protein interactions. In order to achieve this, the RNA stem loop undergoes a concerted rearrangement of the 3' side while leaving the 5' side and the loop interactions largely unchanged, illustrating the ability of RNA to present similar molecular recognition surfaces from distinct primary and secondary structures.
PubMed: 9461079
DOI: 10.1038/nsb0298-133
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

236371

PDB entries from 2025-05-21

PDB statisticsPDBj update infoContact PDBjnumon